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Database: UniProt
Entry: W9XA96_9EURO
LinkDB: W9XA96_9EURO
Original site: W9XA96_9EURO 
ID   W9XA96_9EURO            Unreviewed;       189 AA.
AC   W9XA96;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Small COPII coat GTPase SAR1 {ECO:0000256|ARBA:ARBA00021124};
DE   AltName: Full=Small COPII coat GTPase sar1 {ECO:0000256|ARBA:ARBA00019961};
GN   ORFNames=A1O5_02566 {ECO:0000313|EMBL:EXJ74270.1};
OS   Cladophialophora psammophila CBS 110553.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ74270.1, ECO:0000313|Proteomes:UP000019471};
RN   [1] {ECO:0000313|EMBL:EXJ74270.1, ECO:0000313|Proteomes:UP000019471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ74270.1,
RC   ECO:0000313|Proteomes:UP000019471};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Small GTPase component of the coat protein complex II (COPII)
CC       which promotes the formation of transport vesicles from the endoplasmic
CC       reticulum (ER). The coat has two main functions, the physical
CC       deformation of the endoplasmic reticulum membrane into vesicles and the
CC       selection of cargo molecules. SAR1 controls the coat assembly in a
CC       stepwise manner. Activated SAR1-GTP binds to membranes first and
CC       recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding
CC       intermediates are then collected by the SEC13/31 complex as subunits
CC       polymerize to form coated transport vesicles. Conversion to SAR1-GDP
CC       triggers coat release and recycles COPII subunits.
CC       {ECO:0000256|ARBA:ARBA00025639}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001270};
CC   -!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
CC       complex, the SEC13/31 complex and SAR1.
CC       {ECO:0000256|ARBA:ARBA00011176}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004255}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC       {ECO:0000256|ARBA:ARBA00007507, ECO:0000256|RuleBase:RU003926}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXJ74270.1}.
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DR   EMBL; AMGX01000003; EXJ74270.1; -; Genomic_DNA.
DR   RefSeq; XP_007741370.1; XM_007743180.1.
DR   AlphaFoldDB; W9XA96; -.
DR   STRING; 1182543.W9XA96; -.
DR   GeneID; 19187297; -.
DR   eggNOG; KOG0077; Eukaryota.
DR   HOGENOM; CLU_040729_6_0_1; -.
DR   OrthoDB; 5349301at2759; -.
DR   Proteomes; UP000019471; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   CDD; cd00879; Sar1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   InterPro; IPR006687; Small_GTPase_SAR1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR45684; RE74312P; 1.
DR   PANTHER; PTHR45684:SF2; RE74312P; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51417; ARF; 1.
DR   PROSITE; PS51422; SAR1; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU003926};
KW   ER-Golgi transport {ECO:0000256|RuleBase:RU003926};
KW   Golgi apparatus {ECO:0000256|RuleBase:RU003926};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein transport {ECO:0000256|RuleBase:RU003926};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019471};
KW   Transport {ECO:0000256|RuleBase:RU003926}.
SQ   SEQUENCE   189 AA;  21436 MW;  D9E23312832C96E0 CRC64;
     MWIINWFYDI LASLGLLNKH AKLLFLGLDN AGKTTLLHML KNDRVAILQP TLHPTSEELA
     IGNNRFTTFD LGGHQQARRL WRDYFPEVSG IVFLVDAKDH ERLPEAKAEL DALLAMEDLA
     KTPFLILGNK IDHPDAVSED ELRHQLGLYQ TTGKGKVPLE GIRPIEVFMC SVVMRQGYGE
     GIRWLAQYV
//
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